EA010435B1 - Связывающиеся с tall-1 молекулы и их применение - Google Patents
Связывающиеся с tall-1 молекулы и их применение Download PDFInfo
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- EA010435B1 EA010435B1 EA200301241A EA200301241A EA010435B1 EA 010435 B1 EA010435 B1 EA 010435B1 EA 200301241 A EA200301241 A EA 200301241A EA 200301241 A EA200301241 A EA 200301241A EA 010435 B1 EA010435 B1 EA 010435B1
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/10—Peptides having 12 to 20 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/02—Antineoplastic agents specific for leukemia
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/04—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length on carriers
- C07K1/047—Simultaneous synthesis of different peptide species; Peptide libraries
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/001—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof by chemical synthesis
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4702—Regulators; Modulating activity
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/715—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons
- C07K14/7151—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons for tumor necrosis factor [TNF], for lymphotoxin [LT]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/241—Tumor Necrosis Factors
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display
-
- C—CHEMISTRY; METALLURGY
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B40/00—Libraries per se, e.g. arrays, mixtures
- C40B40/02—Libraries contained in or displayed by microorganisms, e.g. bacteria or animal cells; Libraries contained in or displayed by vectors, e.g. plasmids; Libraries containing only microorganisms or vectors
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Zoology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Toxicology (AREA)
- Biomedical Technology (AREA)
- Wood Science & Technology (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Epidemiology (AREA)
- Cell Biology (AREA)
- Plant Pathology (AREA)
- Crystallography & Structural Chemistry (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Virology (AREA)
- Oncology (AREA)
- Hematology (AREA)
- Transplantation (AREA)
- Dermatology (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US29019601P | 2001-05-11 | 2001-05-11 | |
| PCT/US2002/015273 WO2002092620A2 (en) | 2001-05-11 | 2002-05-13 | Peptides and related molecules that bind to tall-1 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EA200301241A1 EA200301241A1 (ru) | 2004-08-26 |
| EA010435B1 true EA010435B1 (ru) | 2008-08-29 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EA200301241A EA010435B1 (ru) | 2001-05-11 | 2002-05-13 | Связывающиеся с tall-1 молекулы и их применение |
Country Status (30)
| Country | Link |
|---|---|
| US (5) | US7259137B2 (enExample) |
| EP (4) | EP1921088B1 (enExample) |
| JP (1) | JP4516719B2 (enExample) |
| KR (1) | KR100902687B1 (enExample) |
| CN (3) | CN100448891C (enExample) |
| AT (2) | ATE375361T1 (enExample) |
| AU (1) | AU2002342669C1 (enExample) |
| BG (1) | BG66270B1 (enExample) |
| BR (1) | BR0209546A (enExample) |
| CA (1) | CA2446189C (enExample) |
| CY (1) | CY1107131T1 (enExample) |
| CZ (1) | CZ304592B6 (enExample) |
| DE (1) | DE60222882T2 (enExample) |
| DK (1) | DK1385882T3 (enExample) |
| EA (1) | EA010435B1 (enExample) |
| EE (1) | EE05294B1 (enExample) |
| ES (3) | ES2295404T3 (enExample) |
| HK (1) | HK1207390A1 (enExample) |
| HU (1) | HU229910B1 (enExample) |
| IL (2) | IL158719A0 (enExample) |
| MX (1) | MXPA03010210A (enExample) |
| NO (1) | NO331785B1 (enExample) |
| NZ (2) | NZ529267A (enExample) |
| PL (2) | PL210546B1 (enExample) |
| PT (1) | PT1385882E (enExample) |
| RS (1) | RS51708B (enExample) |
| SI (1) | SI1385882T1 (enExample) |
| SK (1) | SK288175B6 (enExample) |
| WO (1) | WO2002092620A2 (enExample) |
| ZA (1) | ZA200308513B (enExample) |
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| US8212004B2 (en) * | 1999-03-02 | 2012-07-03 | Human Genome Sciences, Inc. | Neutrokine-alpha fusion proteins |
| US6812327B1 (en) * | 1996-10-25 | 2004-11-02 | Human Genome Sciences, Inc. | Neutrokine-alpha polypeptides |
| US7879328B2 (en) | 2000-06-16 | 2011-02-01 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to B lymphocyte stimulator |
| NZ522700A (en) * | 2000-06-16 | 2006-02-24 | Human Genome Sciences Inc | Antibodies that immunospecifically bind to blys |
| EP2267018A3 (en) | 2000-08-18 | 2011-04-20 | Human Genome Sciences, Inc. | Binding polypeptides for B lymphocyte stimulator protein (BLyS) |
| WO2002016411A2 (en) | 2000-08-18 | 2002-02-28 | Human Genome Sciences, Inc. | Binding polypeptides and methods based thereon |
| UA83458C2 (uk) | 2000-09-18 | 2008-07-25 | Байоджен Айдек Ма Інк. | Виділений поліпептид baff-r (рецептор фактора активації в-клітин сімейства tnf) |
| MXPA03010210A (es) * | 2001-05-11 | 2004-03-10 | Amgen Inc | Peptidos y moleculas relacionadas que se enlazan a tall-1. |
| US7112410B1 (en) | 2001-08-29 | 2006-09-26 | Human Genome Sciences, Inc. | Human tumor necrosis factor TR21 and methods based thereon |
| AU2003299971A1 (en) | 2002-12-30 | 2004-07-29 | Amgen Inc. | Combination therapy with co-stimulatory factors |
| JP5524441B2 (ja) | 2003-03-28 | 2014-06-18 | バイオジェン・アイデック・エムエイ・インコーポレイテッド | 短縮されたbaffレセプター |
| BRPI0411276A (pt) | 2003-06-05 | 2006-08-01 | Genentech Inc | métodos de esgotamento de células b, método de tratamento de neoplasma de células b ou malignidade, método de alìvio de disfunção autoimunológica regulada por células b, composição e artigo industrializado |
| US7605120B2 (en) * | 2003-10-22 | 2009-10-20 | Amgen Inc. | Antagonists of the brandykinin B1 receptor |
| WO2005075511A1 (en) * | 2004-01-29 | 2005-08-18 | Genentech, Inc. | Variants of the extracellular domain of bcma and uses thereof |
| JP2008503712A (ja) * | 2004-06-21 | 2008-02-07 | ガラパゴス・ナムローゼ・フェンノートシャップ | 骨関節炎治療の方法及び手段 |
| WO2006036834A2 (en) | 2004-09-24 | 2006-04-06 | Amgen Inc. | MODIFIED Fc MOLECULES |
| CN100378122C (zh) * | 2004-12-03 | 2008-04-02 | 中国人民解放军第三军医大学 | B淋巴细胞刺激因子抑制肽及其制备方法 |
| EP1902320B1 (en) | 2005-05-20 | 2010-03-10 | Genentech, Inc. | Pretreatment of a biological sample from an autoimmune disease subject |
| EP3351269B1 (en) | 2005-06-14 | 2020-01-29 | Amgen Inc. | Self-buffering protein formulations |
| US8008453B2 (en) | 2005-08-12 | 2011-08-30 | Amgen Inc. | Modified Fc molecules |
| EA015860B1 (ru) | 2005-10-13 | 2011-12-30 | Хьюман Дженом Сайенсиз, Инк. | Способы лечения аутоиммунных заболеваний при использовании антагониста нейтрокина-альфа |
| US9168286B2 (en) | 2005-10-13 | 2015-10-27 | Human Genome Sciences, Inc. | Methods and compositions for use in treatment of patients with autoantibody positive disease |
| MY149159A (en) | 2005-11-15 | 2013-07-31 | Hoffmann La Roche | Method for treating joint damage |
| EP1952150B1 (en) | 2005-11-23 | 2016-12-14 | Genentech, Inc. | Methods and compositions related to b cell assays |
| WO2007123765A2 (en) | 2006-03-31 | 2007-11-01 | Human Genome Sciences Inc. | Neutrokine-alpha and neutrokine-alpha splice variant |
| JO3324B1 (ar) | 2006-04-21 | 2019-03-13 | Amgen Inc | مركبات علاجية مجففة بالتبريد تتعلق بالعصارة الهضمية |
| US7981425B2 (en) | 2006-06-19 | 2011-07-19 | Amgen Inc. | Thrombopoietic compounds |
| WO2008051383A2 (en) * | 2006-10-19 | 2008-05-02 | Amgen Inc. | Use of alcohol co-solvents to improve pegylation reaction yields |
| AU2008262490B2 (en) | 2007-05-22 | 2011-11-17 | Amgen Inc. | Compositions and methods for producing bioactive fusion proteins |
| US20110097318A1 (en) * | 2007-08-31 | 2011-04-28 | Amgen Inc. | Solid-State Protein Formulation |
| US8383114B2 (en) * | 2007-09-27 | 2013-02-26 | Amgen Inc. | Pharmaceutical formulations |
| EP3381445B1 (en) | 2007-11-15 | 2023-10-25 | Amgen Inc. | Aqueous formulation of antibody stablised by antioxidants for parenteral administration |
| WO2010075249A2 (en) | 2008-12-22 | 2010-07-01 | Genentech, Inc. | A method for treating rheumatoid arthritis with b-cell antagonists |
| US20110014190A1 (en) * | 2009-02-12 | 2011-01-20 | Human Genome Sciences, Inc. | Use of b lymphocyte stimulator protein antagonists to promote transplantation tolerance |
| CA3018235C (en) | 2009-03-20 | 2021-01-12 | Amgen Inc. | Carrier immunoglobulins and uses thereof |
| CN102369215B (zh) | 2009-04-02 | 2015-01-21 | 罗切格利卡特公司 | 包含全长抗体和单链Fab片段的多特异性抗体 |
| MX353186B (es) | 2009-09-03 | 2018-01-05 | Genentech Inc | Metodos para el tratamiento, diagnosis y monitoreo de artritis reumatoide. |
| JP6091894B2 (ja) | 2009-09-16 | 2017-03-15 | ジェネンテック, インコーポレイテッド | コイルドコイルおよび/またはテザー含有タンパク質複合体およびその使用 |
| CA2778105C (en) | 2009-10-23 | 2019-04-02 | Amgen Inc. | Vial adapter and system |
| AR080793A1 (es) | 2010-03-26 | 2012-05-09 | Roche Glycart Ag | Anticuerpos biespecificos |
| RU2624027C2 (ru) | 2010-04-23 | 2017-06-30 | Дженентек, Инк. | Получение гетеромультимерных белков |
| KR20180037303A (ko) | 2010-06-07 | 2018-04-11 | 암젠 인크 | 약물 전달 장치 |
| MX2013001267A (es) | 2010-08-13 | 2013-04-10 | Genentech Inc | ANTICUERPOS A IL-1ß E EIL-18 PARA TRATAMIENTO DE ENFERMEDAD. |
| WO2012025530A1 (en) | 2010-08-24 | 2012-03-01 | F. Hoffmann-La Roche Ag | Bispecific antibodies comprising a disulfide stabilized - fv fragment |
| AU2011305306C1 (en) | 2010-09-22 | 2016-02-18 | Amgen Inc. | Carrier immunoglobulins and uses thereof |
| EP2655413B1 (en) | 2010-12-23 | 2019-01-16 | F.Hoffmann-La Roche Ag | Polypeptide-polynucleotide-complex and its use in targeted effector moiety delivery |
| CN103649117B (zh) | 2011-02-04 | 2016-09-14 | 霍夫曼-拉罗奇有限公司 | Fc变体及其生成方法 |
| US10689447B2 (en) | 2011-02-04 | 2020-06-23 | Genentech, Inc. | Fc variants and methods for their production |
| MX353143B (es) | 2011-02-28 | 2017-12-20 | Genentech Inc | Marcadores biologicos y metodos para pronosticar respuesta a antagonistas de celulas b. |
| AU2012236573B2 (en) | 2011-03-31 | 2016-06-02 | Amgen Inc. | Vial adapter and system |
| US10092706B2 (en) | 2011-04-20 | 2018-10-09 | Amgen Inc. | Autoinjector apparatus |
| DE202012012998U1 (de) | 2011-08-31 | 2014-06-13 | Daniel Elias | Bioaktive, regenerative Mischung zur Herstellung eines Ergänzungsnahrungsmittels |
| PL2766397T3 (pl) | 2011-10-11 | 2018-10-31 | F.Hoffmann-La Roche Ag | Ulepszone składanie przeciwciał bispecyficznych |
| LT3045187T (lt) | 2011-10-14 | 2019-07-10 | Amgen Inc. | Injekcijų įrenginys ir surinkimo būdas |
| EP2809684A1 (en) | 2012-01-31 | 2014-12-10 | Genentech, Inc. | Anti-ig-e m1' antibodies and methods using same |
| RU2644341C2 (ru) | 2012-02-10 | 2018-02-08 | Дженентек, Инк. | Одноцепочечные антитела и другие гетеромультимеры |
| JP6254146B2 (ja) | 2012-03-27 | 2017-12-27 | エヌジーエム バイオファーマシューティカルス,インコーポレーテッド | 代謝障害を治療するための組成物および方法 |
| RU2015100656A (ru) | 2012-06-27 | 2016-08-20 | Ф. Хоффманн-Ля Рош Аг | Способ получения конъюгатов fc-фрагмента антитела, включающих по меньшей мере одну связывающую группировку, которая специфически связывается с мишенью, и их применения |
| CA2871880A1 (en) | 2012-06-27 | 2014-01-03 | F. Hoffmann-La Roche Ag | Method for selection and production of tailor-made highly selective and multi-specific targeting entities containing at least two different binding entities and uses thereof |
| EP3081249B1 (en) | 2012-11-21 | 2020-12-30 | Amgen Inc. | Drug delivery device |
| US9161966B2 (en) | 2013-01-30 | 2015-10-20 | Ngm Biopharmaceuticals, Inc. | GDF15 mutein polypeptides |
| EP2950807B1 (en) | 2013-01-30 | 2018-03-28 | NGM Biopharmaceuticals, Inc. | Compositions and methods of use in treating metabolic disorders |
| PH12022550138A1 (en) | 2013-03-13 | 2023-03-06 | Amgen Inc | Proteins specific for baff and b7rp1 and uses thereof |
| US9458246B2 (en) | 2013-03-13 | 2016-10-04 | Amgen Inc. | Proteins specific for BAFF and B7RP1 |
| EP2968775B1 (en) | 2013-03-15 | 2019-12-18 | Amgen Inc. | Drug cassette, autoinjector, and autoinjector system |
| AU2014228177B2 (en) | 2013-03-15 | 2018-04-26 | Amgen Inc. | Body contour adaptable autoinjector device |
| WO2014144096A1 (en) | 2013-03-15 | 2014-09-18 | Amgen Inc. | Drug cassette, autoinjector, and autoinjector system |
| CA2897825C (en) | 2013-03-22 | 2022-05-24 | Scott R. Gibson | Injector and method of assembly |
| WO2015056356A1 (en) | 2013-10-17 | 2015-04-23 | The Nippon Synthetic Chemical Industry Co., Ltd. | Crosslinkable polymer |
| CA2926110C (en) | 2013-10-24 | 2023-05-23 | Amgen Inc. | Drug delivery system with temperature-sensitive control |
| AU2014340171B2 (en) | 2013-10-24 | 2019-05-30 | Amgen Inc. | Injector and method of assembly |
| WO2015119906A1 (en) | 2014-02-05 | 2015-08-13 | Amgen Inc. | Drug delivery system with electromagnetic field generator |
| WO2015171822A1 (en) | 2014-05-06 | 2015-11-12 | Genentech, Inc. | Production of heteromultimeric proteins using mammalian cells |
| CA3193070A1 (en) | 2014-05-07 | 2015-11-12 | Amgen Inc. | Autoinjector with shock reducing elements |
| KR20170016335A (ko) | 2014-06-03 | 2017-02-13 | 암겐 인코포레이티드 | 약물 전달 디바이스의 사용자를 보조하기 위한 디바이스들 및 방법들 |
| MY192917A (en) | 2014-07-30 | 2022-09-15 | Ngm Biopharmaceuticals Inc | Compositions and methods of use for treating metabolic disorders |
| MX392725B (es) | 2014-10-14 | 2025-03-24 | Amgen Inc | Dispositivo de inyeccion de farmaco con indicadores visuales y audibles. |
| US9920118B2 (en) | 2014-10-31 | 2018-03-20 | Ngm Biopharmaceuticals, Inc. | Compositions and methods of use for treating metabolic disorders |
| EP3227332B1 (en) | 2014-12-03 | 2019-11-06 | F.Hoffmann-La Roche Ag | Multispecific antibodies |
| ES2898469T3 (es) | 2014-12-19 | 2022-03-07 | Amgen Inc | Dispositivo de administración de medicamentos con sensor de proximidad |
| EP3233159B1 (en) | 2014-12-19 | 2020-03-04 | Amgen Inc. | Drug delivery device with live button or user interface field |
| AU2016220141B2 (en) | 2015-02-17 | 2018-07-12 | Amgen Inc. | Drug delivery device with vacuum assisted securement and/or feedback |
| EP3261690B1 (en) | 2015-02-27 | 2021-12-15 | Amgen Inc. | Drug delivery device having a needle guard mechanism with a tunable threshold of resistance to needle guard movement |
| WO2017027861A1 (en) | 2015-08-13 | 2017-02-16 | Amgen Inc. | Charged depth filtration of antigen-binding proteins |
| WO2017039786A1 (en) | 2015-09-02 | 2017-03-09 | Amgen Inc. | Syringe assembly adapter for a syringe |
| ES2755717T3 (es) | 2015-12-09 | 2020-04-23 | Amgen Inc | Autoinyector con tapa de señalización |
| US11154661B2 (en) | 2016-01-06 | 2021-10-26 | Amgen Inc. | Auto-injector with signaling electronics |
| DK3429663T3 (da) | 2016-03-15 | 2020-09-28 | Amgen Inc | Reduktion af sandsynligheden for glasbrud i anordninger til indgivelse af lægemidler |
| CA3016035A1 (en) | 2016-03-31 | 2017-10-05 | Ngm Biopharmaceuticals, Inc. | Binding proteins and methods of use thereof |
| WO2017189089A1 (en) | 2016-04-29 | 2017-11-02 | Amgen Inc. | Drug delivery device with messaging label |
| US11389588B2 (en) | 2016-05-02 | 2022-07-19 | Amgen Inc. | Syringe adapter and guide for filling an on-body injector |
| WO2017197222A1 (en) | 2016-05-13 | 2017-11-16 | Amgen Inc. | Vial sleeve assembly |
| EP3458988B1 (en) | 2016-05-16 | 2023-10-18 | Amgen Inc. | Data encryption in medical devices with limited computational capability |
| EP3465124A1 (en) | 2016-06-03 | 2019-04-10 | Amgen Inc. | Impact testing apparatuses and methods for drug delivery devices |
| US11285266B2 (en) | 2016-07-01 | 2022-03-29 | Amgen Inc. | Drug delivery device having minimized risk of component fracture upon impact events |
| WO2018034784A1 (en) | 2016-08-17 | 2018-02-22 | Amgen Inc. | Drug delivery device with placement detection |
| WO2018081234A1 (en) | 2016-10-25 | 2018-05-03 | Amgen Inc. | On-body injector |
| MX2019008432A (es) | 2017-01-17 | 2019-11-18 | Amgen Inc | Dispositivos de inyeccion y metodos relacionados de uso y ensamblaje. |
| US11752258B2 (en) | 2017-02-17 | 2023-09-12 | Amgen Inc. | Drug delivery device with sterile fluid flowpath and related method of assembly |
| MX2019009755A (es) | 2017-02-17 | 2019-10-07 | Amgen Inc | Mecanismo de insercion para dispositivo de suministro de farmacos. |
| AU2018231107B2 (en) | 2017-03-06 | 2023-04-20 | Amgen Inc. | Drug delivery device with activation prevention feature |
| EP3592402A1 (en) | 2017-03-07 | 2020-01-15 | Amgen Inc. | Needle insertion by overpressure |
| EP3592404A1 (en) | 2017-03-09 | 2020-01-15 | Amgen Inc. | Insertion mechanism for drug delivery device |
| EP4241807B1 (en) | 2017-03-28 | 2025-02-19 | Amgen Inc. | Plunger rod and syringe assembly system |
| US11242397B2 (en) | 2017-06-01 | 2022-02-08 | Pb Immune Therapeutics Inc. | Anti-CD40 antibody and methods for blocking CD40-CD40L signaling |
| AU2018280054B2 (en) | 2017-06-08 | 2023-07-13 | Amgen Inc. | Syringe assembly for a drug delivery device and method of assembly |
| AU2018282077B2 (en) | 2017-06-08 | 2023-11-23 | Amgen Inc. | Torque driven drug delivery device |
| MA49447A (fr) | 2017-06-22 | 2020-04-29 | Amgen Inc | Réduction des impacts/chocs d'activation d'un dispositif |
| WO2018237225A1 (en) | 2017-06-23 | 2018-12-27 | Amgen Inc. | Electronic drug delivery device comprising a cap activated by a switch assembly |
| MA49562A (fr) | 2017-07-14 | 2020-05-20 | Amgen Inc | Système d'insertion-rétractation d'aiguille présentant un système à ressort en double torsion |
| EP3655063A1 (en) | 2017-07-21 | 2020-05-27 | Amgen Inc. | Gas permeable sealing member for drug container and methods of assembly |
| EP3658203B2 (en) | 2017-07-25 | 2025-10-01 | Amgen Inc. | Drug delivery device with gear module and related method of assembly |
| US11484648B2 (en) | 2017-07-25 | 2022-11-01 | Amgen Inc. | Drug delivery device with container access system and related method of assembly |
| MA49838A (fr) | 2017-08-09 | 2020-06-17 | Amgen Inc | Systèm de administration de médicaments avec pression hydraulique-pneumatique de chambre |
| MA49897A (fr) | 2017-08-18 | 2020-06-24 | Amgen Inc | Injecteur sur-corps avec patch adhésif stérile |
| US11103636B2 (en) | 2017-08-22 | 2021-08-31 | Amgen Inc. | Needle insertion mechanism for drug delivery device |
| MA50611A (fr) | 2017-10-04 | 2020-08-12 | Amgen Inc | Adaptateur d'écoulement destiné à un dispositif d'administration de médicament |
| IL272636B2 (en) | 2017-10-06 | 2024-10-01 | Amgen Inc | Drug delivery device with interlock assembly and related method of assembly |
| IL273323B2 (en) | 2017-10-09 | 2024-10-01 | Amgen Inc | Drug delivery device with drive assembly and related assembly method |
| EP3703778A1 (en) | 2017-11-03 | 2020-09-09 | Amgen Inc. | System and approaches for sterilizing a drug delivery device |
| US20200261648A1 (en) | 2017-11-06 | 2020-08-20 | Amgen Inc. | Drug delivery device with placement and flow sensing |
| EP3707075A1 (en) | 2017-11-06 | 2020-09-16 | Amgen Inc. | Fill-finish assemblies and related methods |
| CN111225696B (zh) | 2017-11-10 | 2023-07-18 | 安进公司 | 用于药物递送装置的柱塞 |
| WO2019099324A1 (en) | 2017-11-16 | 2019-05-23 | Amgen Inc. | Door latch mechanism for drug delivery device |
| MX2020005066A (es) | 2017-11-16 | 2020-08-20 | Amgen Inc | Autoinyector con deteccion de detencion y punto final. |
| US10835685B2 (en) | 2018-05-30 | 2020-11-17 | Amgen Inc. | Thermal spring release mechanism for a drug delivery device |
| US11083840B2 (en) | 2018-06-01 | 2021-08-10 | Amgen Inc. | Modular fluid path assemblies for drug delivery devices |
| WO2020023336A1 (en) | 2018-07-24 | 2020-01-30 | Amgen Inc. | Hybrid drug delivery devices with grip portion |
| WO2020023220A1 (en) | 2018-07-24 | 2020-01-30 | Amgen Inc. | Hybrid drug delivery devices with tacky skin attachment portion and related method of preparation |
| WO2020023451A1 (en) | 2018-07-24 | 2020-01-30 | Amgen Inc. | Delivery devices for administering drugs |
| EP3826701A1 (en) | 2018-07-24 | 2021-06-02 | Amgen Inc. | Delivery devices for administering drugs |
| CA3103105A1 (en) | 2018-07-31 | 2020-02-06 | Amgen Inc. | Fluid path assembly for a drug delivery device |
| MA53724A (fr) | 2018-09-24 | 2021-12-29 | Amgen Inc | Systèmes et procédés de dosage interventionnel |
| CA3110371A1 (en) | 2018-09-28 | 2020-04-02 | Amgen Inc. | Muscle wire escapement activation assembly for a drug delivery device |
| AU2019352616B2 (en) | 2018-10-02 | 2024-10-10 | Amgen Inc. | Injection systems for drug delivery with internal force transmission |
| TW202529830A (zh) | 2018-10-05 | 2025-08-01 | 美商安進公司 | 具有劑量指示器之藥物遞送裝置 |
| EA202191037A1 (ru) | 2018-10-15 | 2021-08-05 | Эмджен Инк. | Устройство доставки лекарственного средства, имеющее демпферный механизм |
| SG11202101824VA (en) | 2018-10-15 | 2021-03-30 | Amgen Inc | Platform assembly process for drug delivery device |
| WO2020091956A1 (en) | 2018-11-01 | 2020-05-07 | Amgen Inc. | Drug delivery devices with partial drug delivery member retraction |
| TWI831847B (zh) | 2018-11-01 | 2024-02-11 | 美商安進公司 | 部分針頭縮回之藥物遞送裝置及其操作方法 |
| EP3873563A1 (en) | 2018-11-01 | 2021-09-08 | Amgen Inc. | Drug delivery devices with partial drug delivery member retraction |
| US20220160972A1 (en) | 2019-04-24 | 2022-05-26 | Amgen Inc. | Syringe sterilization verification assemblies and methods |
| WO2021041067A2 (en) | 2019-08-23 | 2021-03-04 | Amgen Inc. | Drug delivery device with configurable needle shield engagement components and related methods |
| EP4341161A1 (en) | 2021-05-21 | 2024-03-27 | Amgen Inc. | Method of optimizing a filling recipe for a drug container |
Family Cites Families (67)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3691016A (en) | 1970-04-17 | 1972-09-12 | Monsanto Co | Process for the preparation of insoluble enzymes |
| CA1023287A (en) | 1972-12-08 | 1977-12-27 | Boehringer Mannheim G.M.B.H. | Process for the preparation of carrier-bound proteins |
| US3941763A (en) | 1975-03-28 | 1976-03-02 | American Home Products Corporation | PGlu-D-Met-Trp-Ser-Tyr-D-Ala-Leu-Arg-Pro-Gly-NH2 and intermediates |
| US4195128A (en) | 1976-05-03 | 1980-03-25 | Bayer Aktiengesellschaft | Polymeric carrier bound ligands |
| US4330440A (en) | 1977-02-08 | 1982-05-18 | Development Finance Corporation Of New Zealand | Activated matrix and method of activation |
| CA1093991A (en) | 1977-02-17 | 1981-01-20 | Hideo Hirohara | Enzyme immobilization with pullulan gel |
| US4229537A (en) | 1978-02-09 | 1980-10-21 | New York University | Preparation of trichloro-s-triazine activated supports for coupling ligands |
| US4289872A (en) | 1979-04-06 | 1981-09-15 | Allied Corporation | Macromolecular highly branched homogeneous compound based on lysine units |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4710473A (en) | 1983-08-10 | 1987-12-01 | Amgen, Inc. | DNA plasmids |
| US4496689A (en) * | 1983-12-27 | 1985-01-29 | Miles Laboratories, Inc. | Covalently attached complex of alpha-1-proteinase inhibitor with a water soluble polymer |
| US4925673A (en) | 1986-08-18 | 1990-05-15 | Clinical Technologies Associates, Inc. | Delivery systems for pharmacological agents encapsulated with proteinoids |
| US5229490A (en) | 1987-05-06 | 1993-07-20 | The Rockefeller University | Multiple antigen peptide system |
| EP0315456B1 (en) | 1987-11-05 | 1994-06-01 | Hybritech Incorporated | Polysaccharide-modified immunoglobulins having reduced immunogenic potential or improved pharmacokinetics |
| US6018026A (en) | 1988-01-22 | 2000-01-25 | Zymogenetics, Inc. | Biologically active dimerized and multimerized polypeptide fusions |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| US5225538A (en) | 1989-02-23 | 1993-07-06 | Genentech, Inc. | Lymphocyte homing receptor/immunoglobulin fusion proteins |
| US5116964A (en) | 1989-02-23 | 1992-05-26 | Genentech, Inc. | Hybrid immunoglobulins |
| US5013556A (en) | 1989-10-20 | 1991-05-07 | Liposome Technology, Inc. | Liposomes with enhanced circulation time |
| US5723286A (en) | 1990-06-20 | 1998-03-03 | Affymax Technologies N.V. | Peptide library and screening systems |
| AU643141B2 (en) | 1991-03-15 | 1993-11-04 | Amgen, Inc. | Pulmonary administration of granulocyte colony stimulating factor |
| US5733731A (en) | 1991-10-16 | 1998-03-31 | Affymax Technologies N.V. | Peptide library and screening method |
| US5270170A (en) | 1991-10-16 | 1993-12-14 | Affymax Technologies N.V. | Peptide library and screening method |
| JPH07505915A (ja) | 1992-04-14 | 1995-06-29 | コーネル リサーチ ファウンデーション、インコーポレーテッド | 樹枝状巨大分子およびその製造法 |
| US5792451A (en) | 1994-03-02 | 1998-08-11 | Emisphere Technologies, Inc. | Oral drug delivery compositions and methods |
| US5417972A (en) * | 1993-08-02 | 1995-05-23 | The Board Of Trustees Of The Leland Stanford Junior University | Method of killing B-cells in a complement independent and an ADCC independent manner using antibodies which specifically bind CDIM |
| US5470952A (en) | 1993-10-20 | 1995-11-28 | Regeneron Pharmaceuticals, Inc. | CNTF and IL-6 antagonists |
| US5922545A (en) | 1993-10-29 | 1999-07-13 | Affymax Technologies N.V. | In vitro peptide and antibody display libraries |
| US6309853B1 (en) | 1994-08-17 | 2001-10-30 | The Rockfeller University | Modulators of body weight, corresponding nucleic acids and proteins, and diagnostic and therapeutic uses thereof |
| DE4435919C1 (de) | 1994-10-07 | 1995-12-07 | Deutsches Krebsforsch | Zinkfinger-DNA, -Protein und ihre Verwendung |
| US5824784A (en) | 1994-10-12 | 1998-10-20 | Amgen Inc. | N-terminally chemically modified protein compositions and methods |
| US5739277A (en) | 1995-04-14 | 1998-04-14 | Genentech Inc. | Altered polypeptides with increased half-life |
| US6096871A (en) | 1995-04-14 | 2000-08-01 | Genentech, Inc. | Polypeptides altered to contain an epitope from the Fc region of an IgG molecule for increased half-life |
| US6127977A (en) | 1996-11-08 | 2000-10-03 | Cohen; Nathan | Microstrip patch antenna with fractal structure |
| WO1997034631A1 (en) | 1996-03-18 | 1997-09-25 | Board Of Regents, The University Of Texas System | Immunoglobin-like domains with increased half lives |
| AU4474497A (en) | 1996-10-08 | 1998-05-05 | U-Bisys B.V. | Methods and means for selecting peptides and proteins having specific affinity for a target |
| CA2266439C (en) | 1996-10-25 | 2009-06-16 | Human Genome Sciences, Inc. | Neutrokine .alpha. |
| US6812327B1 (en) * | 1996-10-25 | 2004-11-02 | Human Genome Sciences, Inc. | Neutrokine-alpha polypeptides |
| WO1999035170A2 (en) | 1998-01-05 | 1999-07-15 | Genentech, Inc. | Compositions and methods for the treatment of tumor |
| AU5705898A (en) | 1996-12-17 | 1998-07-15 | Schering Corporation | Mammalian cell surface antigens; related reagents |
| US5969102A (en) | 1997-03-03 | 1999-10-19 | St. Jude Children's Research Hospital | Lymphocyte surface receptor that binds CAML, nucleic acids encoding the same and methods of use thereof |
| CA2232743A1 (en) | 1997-04-02 | 1998-10-02 | Smithkline Beecham Corporation | A tnf homologue, tl5 |
| CA2292899A1 (en) | 1997-06-06 | 1998-12-10 | Regeneron Pharmaceuticals, Inc. | Ntn-2 member of tnf ligand family |
| EP1012292A1 (en) | 1997-06-06 | 2000-06-28 | Regeneron Pharmaceuticals, Inc. | Ntn-2 member of tnf ligand family |
| WO1999011791A2 (en) | 1997-09-05 | 1999-03-11 | University Of Washington | Tumor necrosis factor family receptors and ligands, encoding nucleic acids and related binding agents |
| KR20010023892A (ko) | 1997-09-12 | 2001-03-26 | 베레이, 헨리 | Kay-신규 면역계 단백질 |
| WO1999062951A1 (en) * | 1998-06-04 | 1999-12-09 | Shanghai Second Medical University | A human zinc finger protein gene (bmzf3) |
| US6660843B1 (en) * | 1998-10-23 | 2003-12-09 | Amgen Inc. | Modified peptides as therapeutic agents |
| EP1642972B1 (en) | 1999-01-07 | 2009-12-30 | ZymoGenetics, Inc. | Therapeutic uses of BR43X2 soluble receptors |
| US20030095967A1 (en) * | 1999-01-25 | 2003-05-22 | Mackay Fabienne | BAFF, inhibitors thereof and their use in the modulation of B-cell response and treatment of autoimmune disorders |
| EA006108B1 (ru) * | 1999-01-25 | 2005-08-25 | Байоджен, Инк. | Способы стимуляции и ингибирования роста в-клеток, продуцирования иммуноглобулинов и коррекции нарушений, связанных с baff-лигандом, у животного |
| AU2880400A (en) | 1999-02-12 | 2000-08-29 | Amgen, Inc. | Tnf-related proteins |
| US20030022233A1 (en) | 1999-04-30 | 2003-01-30 | Raymond G. Goodwin | Methods of use of the taci/taci-l interaction |
| WO2000068378A1 (en) | 1999-05-06 | 2000-11-16 | National Jewish Medical And Research Center | Tall-1 nucleic acid molecules, proteins, receptors and methods of use thereof |
| IL147270A0 (en) | 1999-07-02 | 2002-08-14 | Genentech Inc | Fusion peptides comprising a peptide ligand domain and a multimerization domain |
| US20020160416A1 (en) | 2000-02-11 | 2002-10-31 | Boyle William J. | Receptor from TNF family |
| EP2267018A3 (en) * | 2000-08-18 | 2011-04-20 | Human Genome Sciences, Inc. | Binding polypeptides for B lymphocyte stimulator protein (BLyS) |
| WO2002016411A2 (en) * | 2000-08-18 | 2002-02-28 | Human Genome Sciences, Inc. | Binding polypeptides and methods based thereon |
| MXPA03010210A (es) * | 2001-05-11 | 2004-03-10 | Amgen Inc | Peptidos y moleculas relacionadas que se enlazan a tall-1. |
| AR035119A1 (es) * | 2001-08-16 | 2004-04-14 | Lilly Co Eli | Anticuerpos humanos antagonistas anti-htnfsf13b |
| AU2003299971A1 (en) * | 2002-12-30 | 2004-07-29 | Amgen Inc. | Combination therapy with co-stimulatory factors |
| MX2007000216A (es) * | 2004-07-08 | 2007-03-15 | Amgen Inc | Peptidos terapeuticos. |
| US8008453B2 (en) * | 2005-08-12 | 2011-08-30 | Amgen Inc. | Modified Fc molecules |
| KR101104556B1 (ko) | 2006-12-05 | 2012-01-11 | 가부시키가이샤 고베 세이코쇼 | 인쇄판용 고강도 알루미늄 합금판 |
| PH12022550138A1 (en) * | 2013-03-13 | 2023-03-06 | Amgen Inc | Proteins specific for baff and b7rp1 and uses thereof |
| US9458246B2 (en) * | 2013-03-13 | 2016-10-04 | Amgen Inc. | Proteins specific for BAFF and B7RP1 |
| WO2020175345A1 (ja) | 2019-02-27 | 2020-09-03 | 株式会社村田製作所 | コネクタ、コネクタセット |
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Non-Patent Citations (2)
| Title |
|---|
| Database PNAS, KHARE et al.: Severe B cell hyperplasia and autoimmune disease in TALL-1 transgenis mice. Proc. Natl. Acad. Sci. USA. 28 March 2000, vol. 97, No. 7, p. 3370-3375 * |
| Database PNAS, SHU, H.-B. et al.: B cell maturation protein is a receptor for the tumor necrosis factor family member TALL-1. Proc. Natl. Acad. Sci. USA. 01 August 2000, vol. 97, No. 16, p. 9156-9161 * |
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